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Literature summary for 6.1.1.9 extracted from

  • Hountondji, C.; Schmitter, J.M.; Fukui, T.; Tagaya, M.; Blanquet, S.
    Affinity labeling of aminoacyl-tRNA synthetases with adenosine triphosphopyridoxal. Probing the Lys-Met-Ser-Lys-Ser signature sequence as the ATP-binding site in Escherichia coli methionyl- and valyl-tRNA synthetases (1990), Biochemistry, 29, 11266-11273.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
pyridoxal 5'-triphospho-5'-adenosine aminoacylation and ATP-diphosphate exchange abolished Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-valine + tRNAVal
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Escherichia coli AMP + diphosphate + L-valyl-tRNAVal
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additional information valine-dependent ATP-diphosphate exchange: valine + ATP + enzyme /Val-AMP-enzyme + diphosphate Escherichia coli ?
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